We study the structural differences between members of large metalloenzyme superfamilies that share common features but promote different reactions or use distinct cofactors. Our targets are unified in their ability to activate strong C-H, N-H, or O-H bonds. We have three overarching objectives:
1) identification of the key outcome-dictating structural characteristics of a given catalyst
2) reprogramming for new function using insight from structure
3) understanding the adaptive advantages in choice of metallocofactor or assembly pathway.
We characterize stable reactant and product complexes to answer these questions, with an increasing focus on development and implementation of crystallographic approaches to study metalloenzyme reaction intermediates.